The Fbe (SdrG) protein of Staphylococcus epidermidis HB promotes bacterial adherence to fibrinogen.

Staphylococcus epidermidis strains HB and K28 express surface proteins called Fbe or SdrG, respectively, that have sequence similarity to the clumping factors ClfA and ClfB of Staphylococcus aureus. A mutation in the fbe gene of strain HB was isolated by directed plasmid integration using the broad-host-range temperature-sensitive plasmid pG(+)Host9 (pVE6155). An internal fragment of fbe was cloned into pG(+)Host9 and the chimaeric plasmid was mobilized from S.

The serine-aspartate repeat (Sdr) protein family in Staphylococcus epidermidis.

Staphylococcus epidermidis can express three different cell-surface-associated proteins, designated SdrF, SdrG and SdrH, that contain serine-aspartate dipeptide repeats. Proteins SdrF and SdrG are similar in sequence and structural organization to the Sdr proteins of Staphylococcus aureus and comprise unique 625- and 548-residue A regions at their N termini, respectively, followed by 110-119-residue B-repeat regions and SD-repeat regions. The C termini contain LPXTG motifs and hydrophobic amino acid segments characteristic of surface proteins covalently anchored to peptidoglycan.

Matrix-binding proteins of Staphylococcus aureus: functional analysis of mutant and hybrid molecules.

The fibrinogen-binding protein ClfA and the collagen-binding protein Cna are surface-associated adhesins of Staphylococcus aureus. ClfA has a dipeptide repeat region R composed mainly of serine and aspartate residues, more than 40 of which are required along with the 28-residue region W, the LPXTG motif and region M to display the ligand-binding region A on the cell surface in a functional form. Cna has a 61-residue region W and at least one 187-residue region B linking the collagen-binding region A to peptidoglycan.